Wound-induced accumulation of mRNA containing a hevein sequence in laticifers of rubber tree (Hevea brasiliensis).

Broekaert, Willem F.; Lee, Hyung‐il; Kush, Anil; Chua, Nam‐Hai; Raikhel, Natasha V.

doi:10.1073/pnas.87.19.7633

Cited by 260 publications

(160 citation statements)

References 33 publications

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“…It is identical to residues 159-173 corresponding to the cDNA sequence of the hevein precursor [4], except for the two underlined residues, which are Ile and Asp, respectively, in the latter. We do not know the cause of these differences.…”

Section: Resultsmentioning

confidence: 90%

“…Broekaert et al [4] have determined its cDNA sequence and found that it is synthesized as a precursor with a signal sequence of 17 residues, followed by the hevein domain of 43 residues and a C-terminal region of 144 residues. The C-terminal domain and the precursor consisting of the hevein and the C-terminal domain are also present in the lutoid-body fraction of latex [5].…”

Section: Introductionmentioning

confidence: 99%

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Processed products of the hevein precursor in the latex of the rubber tree (Hevea brasiliensis)

1995

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The 20 kDa precursor of hevein and its C-terminal 14 kDa domain have been isolated. Sequence analysis of the Cterminal tryptic peptides of these proteins and comparison with the cDNA sequence indicate that they represent mature forms from which a C-terminal propeptide, possibly involved in vacuolar targeting, has been removed. The molar ratio of hevein to the C-terminal domain in the lutoid-body fraction of rubber latex is about 30:1. This indicates that not only the pre-and propeptides but also the 14 kDa domain are removed by proteolysis or other processes in the latex vessel after the processing of hevein has taken place.the hevein domain in this protein is not cleaved off in the mature form.Here we report the isolation of the hevein precursor and its C-terminal domain and present evidence that they are the mature proteins from which a C-terminal propeptide has already been removed. The large molar excess of hevein in the lutoidbody fraction of rubber latex indicates that much proitein turnover occurs in the latex vessels of the rubber tree. Materials and methods

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Section: Resultsmentioning

confidence: 90%

Section: Introductionmentioning

confidence: 99%

Processed products of the hevein precursor in the latex of the rubber tree (Hevea brasiliensis)

1995

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“…The sequence is very similar to that of the protein hevein (isolated from rubber tree latex) which folds into a 'toxin-agglutinin fold' or 'hevein domain' [2]. Structure determination of hevein by ~H NMR [3] and of WGA by X-ray diffraction [4] have shown that the WGA domains and hevein have a common structural fold.…”

Section: Introductionmentioning

confidence: 73%

¹H NMR study of the interaction ofN,N′,N″‐triacetyl chitotriose with Ac‐AMP2, a sugar binding antimicrobial protein isolated fromAmaranthus caudatus

et al. 1995

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“…Among them, the hevein-like peptides, such as hevein from laticifers of rubber tree (4,5), antimicrobial peptides from Amaranthus caudatus seeds (Ac-AMP) (6,7), and antifungal peptides from the seeds of Pharbitis nil (Pn-AMP) (8), have specific chitin-binding activities and are characterized by three or four disulfides to stabilize a chitin-binding domain referred as hevein domain (2,9) as shown in Figure 1. This hevein domain mostly consists of 30-43 residues including six or eight cysteines pairing into three or four disulfide bonds, three aromatic residues, two glycines, and one serine ( Figure 1) and occurs in a variety of plant proteins and peptides in multiple or single copies, respectively (2).…”

mentioning

confidence: 99%

Solution Structure of Eucommia Antifungal Peptide: A Novel Structural Model Distinct with a Five-Disulfide Motif^,

Huang

Xiang

et al. 2004

Biochemistry

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The three-dimensional structure in aqueous solution of Eucommia antifungal peptide 2 (EAFP2) from Eucommia ulmoides Oliv was determined using 1 H NMR spectroscopy. EAFP2 is a newly discovered 41-residue peptide distinct with a five-disulfide cross-linked motif. This peptide exhibits chitin-binding activity and inhibitory effects on the growth of cell wall chitin-containing fungi and chitin-free fungi. The structure was calculated by using torsion angle dynamic simulated annealing with a total of 614 distance restraints and 16 dihedral restraints derived from NOESY and DQF-COSY spectra, respectively. The five disulfide bonds were assigned from preliminary structures using a statistical analysis of intercystinyl distances. The solution structure of EAFP2 is presented as an ensemble of 20 conformers with a backbone RMS deviation of 0.65 ((0.13) Å for the well-defined Cys3-Cys39 segment. The tertiary structure of EAFP2 represents the first five-disulfide cross-linked structural model of the plant antifungal peptide. EAFP2 adopts a compact global fold composed of a 3 10 helix (Cys3-Arg6), an R-helix (Gly26-Cys30), and a three-strand antiparallel -sheet (Cys16-Ser18, Tyr22-Gly24, and Arg36-Cys37). The tertiary structure of EAFP2 shows a chitin-binding domain (residues 11-30) with a hydrophobic face and a characteristic sector formed by the N-terminal 10 residues and the C-terminal segment cross-linked through the unique disulfide bond Cys7-Cys37, which brings all four positively charged residues (Arg6, Arg9, Arg36, and Arg40) onto a cationic face. On the basis of such a structural feature, the possible structural basis for the functional properties of EAFP2 is discussed.

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Wound-induced accumulation of mRNA containing a hevein sequence in laticifers of rubber tree (Hevea brasiliensis).

Abstract: Hevein is a chitin-binding protein that is present in laticifers of the rubber tree (Hevea brasilensis

Cited by 260 publications

References 33 publications

Processed products of the hevein precursor in the latex of the rubber tree (Hevea brasiliensis)

Processed products of the hevein precursor in the latex of the rubber tree (Hevea brasiliensis)

¹H NMR study of the interaction ofN,N′,N″‐triacetyl chitotriose with Ac‐AMP2, a sugar binding antimicrobial protein isolated fromAmaranthus caudatus

Solution Structure of Eucommia Antifungal Peptide: A Novel Structural Model Distinct with a Five-Disulfide Motif^,

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Wound-induced accumulation of mRNA containing a hevein sequence in laticifers of rubber tree (Hevea brasiliensis).

Abstract: Hevein is a chitin-binding protein that is present in laticifers of the rubber tree (Hevea brasilensis

Cited by 260 publications

References 33 publications

Processed products of the hevein precursor in the latex of the rubber tree (Hevea brasiliensis)

Processed products of the hevein precursor in the latex of the rubber tree (Hevea brasiliensis)

1H NMR study of the interaction ofN,N′,N″‐triacetyl chitotriose with Ac‐AMP2, a sugar binding antimicrobial protein isolated fromAmaranthus caudatus

Solution Structure of Eucommia Antifungal Peptide: A Novel Structural Model Distinct with a Five-Disulfide Motif,

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¹H NMR study of the interaction ofN,N′,N″‐triacetyl chitotriose with Ac‐AMP2, a sugar binding antimicrobial protein isolated fromAmaranthus caudatus

Solution Structure of Eucommia Antifungal Peptide: A Novel Structural Model Distinct with a Five-Disulfide Motif^,